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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 15120001
Publication DOI: 10.1179/09680510422500400
Journal NLM ID: 9433350
Publisher: Maney Publishing
Correspondence: russell.bishop

utoronto.ca
Institutions: Departments of Laboratory Medicine and Pathobiology, and Biochemistry, University of Toronto, Toronto, Ontario, Canada

The enzymology of palmitate addition to lipid A can be traced to the early discovery of monosaccharide lipid A precursors, but the functional importance of lipid A palmitoylation in bacterial resistance to the host immune response has emerged only recently. Lipid A palmitoylation in enterobacteria is determined by a PhoP/PhoQ-activated gene pagP, which encodes an unusual outer membrane enzyme of lipid A biosynthesis. PagP structure and dynamics have now been elucidated by both NMR spectroscopy and X-ray crystallography. PagP is an 8-stranded antiparallel Я-barrel preceded by an N-terminal amphipathic a-helix. The PagP barrel axis is uniquely tilted by 30° with respect to the membrane normal. An interior hydrophobic pocket in the upper half of the molecule functions as a hydrocarbon ruler, which allows the enzyme to distinguish palmitate from other acyl chains found in phospholipids. Internalization of a phospholipid palmitoyl group within the barrel appears to occur by lateral diffusion from the outer leaflet through non-hydrogen bonded regions between Я-strands. The MsbA-dependent trafficking of lipids from the inner membrane to the outer membrane outer leaflet is necessary for lipid A palmitoylation in vivo. Efforts to determine the PagP catalytic mechanism may lead to the development of inhibitors for the treatment of infections.

Lipid A palmitoylation, enzymology, PagP

Structure type: oligomer
Location inside paper: p.108, fig.1, hepta-acylated Kdo2-lipid A
Trivial name: hepta-acylated Kdo2-lipid A, C16-Kdo2-lipid A
Compound class: lipid A
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141181,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_534864

Methods: genetic methods, biochemical methods
Enzymes that release or process the structure: PagP
Comments, role: Proceedings paper; lipid A palmitoylation

Related record ID(s): 9543
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases

There is only one chemically distinct structure:

CCCCCCCCCCCCCCCC(=O)O[C@H](CCCCCCCCCCC)CC(=O)N[C@H]1[C@@H](OP(=O)(O)O)O[C@H](CO[C@@H]2O[C@H](CO[C@]3(C(=O)O)C[C@@H](O[C@]4(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O4)[C@@H](O)[C@@H]([C@H](O)CO)O3)[C@@H](OP(=O)(O)O)[C@H](OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC)[C@H]2NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC)[C@@H](O)[C@@H]1OC(=O)C[C@H](O)CCCCCCCCCCC

SVG MW SMILES 3D mol Ionize